Abstract:
:To investigate the molecular interactions of synaptophysin I and vesicle-associated membrane protein 2 (VAMP2)/synaptobrevin II during exocytosis, we have used time-lapse videomicroscopy to measure fluorescence resonance energy transfer in live neurons. For this purpose, fluorescent protein variants fused to synaptophysin I or VAMP2 were expressed in rat hippocampal neurons. We show that synaptophysin I and VAMP2 form both homo- and hetero-oligomers on the synaptic vesicle membrane. When exocytosis is stimulated with alpha-latrotoxin, VAMP2 dissociates from synaptophysin I even in the absence of appreciable exocytosis, whereas synaptophysin I oligomers disassemble only upon incorporation of the vesicle with the plasma membrane. We propose that synaptophysin I has multiple roles in neurotransmitter release, regulating VAMP2 availability for the soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex and possibly participating in the late steps of exocytosis.
journal_name
Mol Biol Celljournal_title
Molecular biology of the cellauthors
Pennuto M,Dunlap D,Contestabile A,Benfenati F,Valtorta Fdoi
10.1091/mbc.e02-01-0036keywords:
subject
Has Abstractpub_date
2002-08-01 00:00:00pages
2706-17issue
8eissn
1059-1524issn
1939-4586journal_volume
13pub_type
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